• 제목/요약/키워드: protein structure

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Apriona germari Larval Cuticle Protein Genes: Genomic Structure of Three Cuticle Protein Genes and cDNA Cloning of a Novel Cuticle Protein

  • Zheng Gui Zhong;Kim Bo-Yeon;Yoon Hyung-Joo;Wei Ya Dong;Xijie Guo;Jin Byung-Rae;Shon Hung-Dae
    • International Journal of Industrial Entomology and Biomaterials
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    • 제14권1호
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    • pp.51-56
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    • 2007
  • In a previous study, three larval cuticle protein genes were cloned from the mulberry longicorn beetle, Apriona germari (Comp. Biochem. Physiol. B 136, 803-811, 2003). In the present study, the genomic structures of these three larval cuticle protein genes (AgLCP9.2, AgLCP12.6 and AgLCP12.3) were elucidated. All three cuticle protein genes consist of one intron and two exons. Southern blot analysis of genomic DNA suggested that three cuticle protein genes are a single copy gene. In addition, a novel larval cuticle protein gene, AgLCP10.6, was cloned from A. germari in this study. The AgLCP10.6 cDNA contains an ORF of 300 nucleotides that are capable of encoding a 100-amino acid polypeptide with a predicted molecular mass of 10.6 kDa. The amino acid sequence deduced from the AgLCP10.6 cDNA contained a type-specific consensus sequence identifiable in other insect cuticle proteins and is most homologous to Drosophila melanogaster cuticle protein ACP65A (51 % protein sequence identity). Northern blot analysis revealed that AgLCP10.6 showed epidermis-specific expression.

Molecular characterization and functional annotation of a hypothetical protein (SCO0618) of Streptomyces coelicolor A3(2)

  • Ferdous, Nadim;Reza, Mahjerin Nasrin;Emon, Md. Tabassum Hossain;Islam, Md. Shariful;Mohiuddin, A.K.M.;Hossain, Mohammad Uzzal
    • Genomics & Informatics
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    • 제18권3호
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    • pp.28.1-28.9
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    • 2020
  • Streptomyces coelicolor is a gram-positive soil bacterium which is well known for the production of several antibiotics used in various biotechnological applications. But numerous proteins from its genome are considered hypothetical proteins. Therefore, the present study aimed to reveal the functions of a hypothetical protein from the genome of S. coelicolor. Several bioinformatics tools were employed to predict the structure and function of this protein. Sequence similarity was searched through the available bioinformatics databases to find out the homologous protein. The secondary and tertiary structure were predicted and further validated with quality assessment tools. Furthermore, the active site and the interacting proteins were also explored with the utilization of CASTp and STRING server. The hypothetical protein showed the important biological activity having with two functional domain including POD-like_MBL-fold and rhodanese homology domain. The functional annotation exposed that the selected hypothetical protein could show the hydrolase activity. Furthermore, protein-protein interactions of selected hypothetical protein revealed several functional partners those have the significant role for the bacterial survival. At last, the current study depicts that the annotated hypothetical protein is linked with hydrolase activity which might be of great interest to the further research in bacterial genetics.

Cytochrome c Peroxidase: A Model Heme Protein

  • Erman, James E.;Vitello, Lidia B.
    • BMB Reports
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    • 제31권4호
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    • pp.307-327
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    • 1998
  • Cytochrome c peroxidase (CcP) is a yeast mitochondrial enzyme which catalyzes the reduction of hydrogen peroxide to water using two equivalents of ferrocytochrome c. The CcP/cytochrome c system has many features which make it a very useful model for detailed investigation of heme protein structure/function relationships including activation of hydrogen peroxide, protein-protein interactions, and long-range electron transfer. Both CcP and cytochrome c are single heme, single subunit proteins of modest size. High-resolution crystallographic structures of both proteins, of one-to-one complexes of the two proteins, and a number of active-site mutants are available. Site-directed mutagenesis studies indicate that the distal histidine in CcP is primarily responsible for rapid utilization of hydrogen peroxide implying significantly different properties of the distal histidine in the peroxidases compared to the globins. CcP and cytochrome c bind to form a dynamic one-to-one complex. The binding is largely electrostatic in nature with a small, unfavorable enthalpy of binding and a large positive entropy change upon complex formation. The cytochrome c-binding site on CcP has been mapped in solution by measuring the binding affinities between cytochrome c and a number of CcP surface mutations. The binding site for cytochrome c in solution is consistent with the crystallographic structure of the one-to-one complex. Evidence for the involvement of a second, low-affinity cytochrome c-binding site on CcP in long-range electron transfer between the two proteins is reviewed.

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Structural Characterization of the J-domain of Tid1, a Mitochondrial Hsp40/DnaJ Protein

  • Sim, Dae-Won;Jo, Ku-Sung;Ryu, Kyoung-Seok;Kim, Eun-Hee;Won, Hyung-Sik
    • 한국자기공명학회논문지
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    • 제16권1호
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    • pp.22-33
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    • 2012
  • Tid1, belonging to the Hsp40/DnaJ family of proteins, functions as a cochaperone of cytosolic and mitochondrial Hsp70 proteins. In particular, the N-terminal J-domain of Tid1 (Tid1-JD) constitutes the major binding sites for proteinprotein interactions with client proteins, including p53, as well as its partner chaperone, Hsp70. In the present study, soluble, recombinant protein of Tid1-JD could be obtained by using the pCold vector system, and backbone NMR assignments were completed using the isotope $[^{13}C/^{15}N]$-enriched protein. Far-UV CD result implied that Tid1-JD is an ${\alpha}$-helical protein and the secondary structure determined using chemical shift data sets indentified four ${\alpha}$-helices with a loop region containing the HPD (conserved tripeptide of His, Pro and Asp) motif. Additionally, NMR spectra under different conditions implied that the HPD motif, which is a critical region for protein-protein interactions of Tid1-JD, would possess dynamic properties.

Solution Structure of YKR049C, a Putative Redox Protein from Saccharomyces cerevisiae

  • Jung, Jin-Won;Yee, Adelinda;Wu, Bin;Arrowsmith, Cheryl H.;Lee, Weon-Tae
    • BMB Reports
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    • 제38권5호
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    • pp.550-554
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    • 2005
  • YKR049C is a mitochondrial protein in Saccharomyces cerevisiae that is conserved among yeast species, including Candida albicans. However, no biological function for YKR049C has been ascribed based on its primary sequence information. In the present study, NMR spectroscopy was used to determine the putative biological function of YKR049C based on its solution structure. YKR049C shows a well-defined thioredoxin fold with a unique insertion of helices between two $\beta$-strands. The central $\beta$-sheet divides the protein into two parts; a unique face and a conserved face. The 'unique face' is located between ${\beta}2$ and ${\beta}3$. Interestingly, the sequences most conserved among YKR049C families are found on this 'unique face', which incorporates L109 to E114. The side chains of these conserved residues interact with residues on the helical region with a stretch of hydrophobic surface. A putative active site composed by two short helices and a single Cys97 was also well observed. Our findings suggest that YKR049C is a redox protein with a thioredoxin fold containing a single active cysteine.

여러가지 단백질 첨가로 인한 두부의 특성변화 (The Characteristic Changes of Soybean Curds by Addition of Several Types of Protein)

  • 변진원;황인경
    • 한국식품조리과학회지
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    • 제6권3호통권12호
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    • pp.33-41
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    • 1990
  • This study was conducted to compare the characteristics of the ordinary soybean curd and 3 protein-adding soybean curds (soy protein, casein, gelatin). The sensory evaluation, textural analysis by Instron Universal Testing Machine & the microstructure analysis by SEM for 4 soybean curds were carried out. The results were as follows: 1. In sensory evaluation. 1) The differentiation of soybean curds was greatly explained by `hardness in mouth' through ANOVA test. 2) Discriminant analysis showed that the properties of casein soybean curd were different from those of other three soybean curds by discriminant function I, and the properties of soy protein soybean curd were slightly different from those of ordinary and gelatin soybean curds by discriminant function II. 2. In textural analysis by Instron, protein-adding soybean curds showed significantly lower hardness than ordinary soybean curd. 3. In microstructure analysis by SEM, soy protein soybean curd showed regular, good honeycomb-like network structure and other soybean curds showed lumpy network. The structure of gelatin soybean curd was slightly similar to that of ordinary soybean curd.

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생리활성 성분을 처방한 헤어토너가 탈색모발에 미치는 영향 (Effects of Hair Toner Formulated with Bioactive Substances on Bleached Hair)

  • 박선화;안춘순
    • 한국의류학회지
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    • 제46권3호
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    • pp.494-512
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    • 2022
  • Hair toners containing polyphenol or Vitamin B5 were investigated according to their recovering effects on hair damaged by bleaching. Surface morphology, CIE L*a*b* values, and tensile properties of hair were measured. The amount of protein leaking from hair was investigated using the Bradford protein assay. The amino acid composition of hair was examined using the HPLC instrument. Hair became severely damaged after bleaching, showing cuticle structure with surface melt down and rolled up tip, a decrease in tensile strength, an increase in protein leak, and an increase in the proportion of cysteic acid. When bleached hair was treated with the two types of hair toner, positive effects were seen in the recovery of cuticle structure and retention of bleached color, an increase in tensile strength, a decrease in protein leak up to certain days, and an increase in the retention of protein examined by the HPLC analysis of amino acids. Hair treated with B5 toner showed better effects on the increase of tensile strength compared to the hair treated with PP toner. Hair treated with PP toner showed better retention of color, less protein leak, and a lower proportion of cysteic acid compared to the hair treated with B5 toner.

Protein Secondary Structure Prediction using Multiple Neural Network Likelihood Models

  • Kim, Seong-Gon;Kim, Yong-Gi
    • International Journal of Fuzzy Logic and Intelligent Systems
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    • 제10권4호
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    • pp.314-318
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    • 2010
  • Predicting Alpha-helicies, Beta-sheets and Turns of a proteins secondary structure is a complex non-linear task that has been approached by several techniques such as Neural Networks, Genetic Algorithms, Decision Trees and other statistical or heuristic methods. This project introduces a new machine learning method by combining Bayesian Inference with offline trained Multilayered Perceptron (MLP) models as the likelihood for secondary structure prediction of proteins. With varying window sizes of neighboring amino acid information, the information is extracted and passed back and forth between the Neural Net and the Bayesian Inference process until the posterior probability of the secondary structure converges.

On the Crystal Structure of a human Cell Division Cycle Controlling Protein Kinase(CDK2) and Structure-Based Drug Design

  • Kim, Sung-Hou-
    • 한국응용약물학회:학술대회논문집
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    • 한국응용약물학회 1994년도 춘계학술대회 and 제3회 신약개발 연구발표회
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    • pp.41-49
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    • 1994
  • The most common conventional method of discovering a drug involves a massive screening of a large number of compounds in chemical libraries or in the extracts from natural sources such as plants or microbial broths followed by chemical modification of one or more active compounds to improve their properties as a drug. When the three-dimensional structure of the target molecule for which the drug is searched is known the drug discovery process can be significantly simplified, This is especially true when the three-dimensional structure of a complex between the target and a lead compound is known. In this lecture our experience on the structure-based drug design for human CDK2(cyclin-dependent protein kinase 2) will be discussed with special emphasis on the strength and weakness of this approach of drug discovery. The regulation of the activity of CDK2 plays an important role in the cell proliferation of normal and cancer cells.

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Theoretical Investigations on Structure and Function of Human Homologue hABH4 of E.coli ALKB4

  • Shankaracharya, Shankaracharya;Das, Saibal;Prasad, Dinesh;Vidyarthi, Ambarish Sharan
    • Interdisciplinary Bio Central
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    • 제2권3호
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    • pp.8.1-8.5
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    • 2010
  • Introduction: Recently identified human homologues of ALKB protein have shown the activity of DNA damaging drugs, used for cancer therapy. Bioinformatics study of hABH2 and hABH3 had led to the discovery of a novel DNA repair mechanism. Very little is known about structure and function of hABH4, one of the members of this superfamily. Therefore, in present study we are intended to predict its structure and function through various bioinformatics tools. Materials and Methods: Modeling was done with modeler 9v7 to predict the 3D structure of the hABH4 protein. This model was validated with the program Procheck using Ramachandran plot statistics and was submitted to PMDB with ID PM0076284. The 3d2GO server was used to predict the functions. Residues at protein ligand and protein RNA binding sites were predicted with 3dLigandSite and KYG programs respectively. Results and Discussion: 3-D model of hABH4, ALKBH4.B99990003.pdb was predicted and evaluated. Validation result showed that 96.4 % residues lies in favored and additional allowed region of Ramachandran plot. Ligand binding residues prediction showed four Ligand clusters, having 24 ligands in cluster 1. Importantly, conserved pattern of Glu196-X-Pro198- Xn-His254 in the functional domain was detected. DNA and RNA binding sites were also predicted in the model. Conclusion and Prospects: The predicted and validated model of human homologue hABH4 resulted from this study may unveil the mechanism of DNA damage repair in human and accelerate the research on designing of appropriate inhibitors aiding in chemotherapy and cancer related diseases.